We have been able to specifically label the phospholipid head groups and acyl chains of vesicles, liposomes and intact cells. This enrichment has enabled us to obtain high quality 13C (67.8 MHz) and 2H (41.4 MHz) NMR spectra of these systems. We have examined the effect of temperature, cholesterol and/or protein concentration on the spectra and have found striking changes which reflect changes in the phospholipid head group and acyl chain motions and ordering. We propose to use high field NMR spectroscopy as a non-perturbative method to compare the motions and topography of 13C and 2H labeled phospholipids in plasma membranes from normal and virus-transformed cell populations derived from identical cell lines. NMR parameters which will be measured--2H order parameters, 13C relaxation times (T1, T2) will be used to study the ordering and rates of motion of the membrane phospholipids. In addition, we will use shift reagents to study the topography of phospholipids in normal and transformed cell membranes. We will compare the following systems derived from the normal and transformed cell populations: (1) envelopes of viral particles (Sindbis, vesicular stomatitis) which have budded through the host plasma membranes; (2) vesicles and liposomes comprised of lipids extracted from the viral envelopes and from the isolated host plasma membranes; (3) the isolated host plasma membranes; (4) the plasma membranes of intact cells. We plan to carry out the experiments in the order listed above, proceeding in a series of stages from the simplest (i.e., virus) to the most complex systems (i.e., intact cells).